Table 2.
Summary of ACTase activity characteristics in H. pylori
| Enzyme characteristic | Data from H. pylori ACTase |
| Km (carbamoyl phosphate) | 0.6 mM |
| Km (L-aspartate) | 11.6 mM |
| Vmax (carbamoyl phosphate) | 0.68 μmole min-1 (mg protein)-1 |
| Vmax (L-aspartate) | 0.64 μmole min-1 (mg protein)-1 |
| pH optimum | 8.0 |
| Temperature optimum | 45°C |
| Substrate specificity | Specific for L-aspartate |
| Effect of aspartate analogues | Succinate and malate inhibit |
| Effect of phosphate analogues | Phosphonoacetate and acetyl phosphate inhibit |
| Effect of PALA | 50% inhibition at 0.1 μM; Ki of 0.245 μM |
| Effect of nucleotides | All, tri-, di-, and monophosphate nucleotides inhibit |